title: Myoglobin on silica: a case study of the impact of adsorption on protein structure and dynamics.
abstract: If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low frequency modes of myoglobin after adsorption on silica was observed. Our results suggest that the structure loss itself is not the entropic driving force of adsorption.
authors.affiliation: Laboratoire de Radiolyse, SIS2M, IRAMIS, UMR3299 CEA-CNRS , 91191 Gif-sur-Yvette, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Devineau
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Zanotti
authors.forename: Camille
authors.initials: C
authors.lastname: Loupiac
authors.forename: Loussiné
authors.initials: L
authors.lastname: Zargarian
authors.forename: Fabrice
authors.initials: F
authors.lastname: Neiers
authors.forename: Serge
authors.initials: S
authors.lastname: Pin
authors.forename: Jean Philippe
authors.initials: JP
authors.lastname: Renault
mesh_terms: D000327:Adsorption; D000818:Animals; D008786:Metmyoglobin / Q000737:chemistry* / Q000378:metabolism*; D053758:Nanoparticles / Q000737:chemistry; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D008786:Metmyoglobin; D012822:Silicon Dioxide